about
A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolutionForce-induced remodelling of proteins and their complexesLighting Up the Force: Investigating Mechanisms of Mechanotransduction Using Fluorescent Tension Probes.Engineering broadly neutralizing antibodies for HIV prevention and therapy.The influence of disulfide bonds on the mechanical stability of proteins is context dependent.Mechanical architecture and folding of E. coli type 1 pilus domains.
P2860
description
2014 nî lūn-bûn
@nan
2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Probing the effect of force on HIV-1 receptor CD4.
@ast
Probing the effect of force on HIV-1 receptor CD4.
@en
Probing the effect of force on HIV-1 receptor CD4.
@nl
type
label
Probing the effect of force on HIV-1 receptor CD4.
@ast
Probing the effect of force on HIV-1 receptor CD4.
@en
Probing the effect of force on HIV-1 receptor CD4.
@nl
prefLabel
Probing the effect of force on HIV-1 receptor CD4.
@ast
Probing the effect of force on HIV-1 receptor CD4.
@en
Probing the effect of force on HIV-1 receptor CD4.
@nl
P2093
P2860
P50
P356
P1433
P1476
Probing the effect of force on HIV-1 receptor CD4.
@en
P2093
Carmen L Badilla
David Franco
Julio M Fernandez
Ming-Wei Chen
Patricia Richard
P2860
P304
10313-10320
P356
10.1021/NN503557W
P407
P577
2014-10-14T00:00:00Z